Protein Family Models

This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure [1-2]. [1]. 8804825. Structural classification of proteins: new superfamilies. Murzin AG;. Curr Opin Struct Biol 1996;6:386-394. [2]. 10556240. Conserved structural features and sequence patterns in the GroES fold family. Taneja B, Mande SC;. Protein Eng 1999;12:815-818. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Gene:

frmA

Date:

2020-01-25

S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase catalyzes the zinc-dependent conversion of formaldehyde and NAD(P) to formate and NAD(P)H, via the formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione; belongs to the medium chain dehydrogenase/reductase (MDR) family

Date:

2023-03-01

The members of this protein family show dual function. First, they remove formaldehyde, a toxic metabolite, by acting as S-(hydroxymethyl)glutathione dehydrogenase (1.1.1.284). S-(hydroxymethyl)glutathione can form spontaneously from formaldehyde and glutathione, and so this enzyme previously was designated glutathione-dependent formaldehyde dehydrogenase. These same proteins are also designated alcohol dehydrogenase (EC 1.1.1.1) of class III, for activities that do not require glutathione; they tend to show poor activity for ethanol among their various substrate alcohols.

Date:

2024-10-21